A roadmap for HLA-DR peptide binding specificities.
Peptide residue positional environments have previously been defined for class I MHC allelic products. These environments provide a less restrictive description of the traditional peptide binding pockets of class I molecules. When combined with the peptide anchor motifs that have been identified for some class I molecules, predictions as to likely motifs for other MHC molecules, which share the same potential environment can be made. Here, the same approach is used to derive peptide residue positional environments for class II MHC molecules. The environments are used to make predictions as to likely binding motifs for HLA-DR allelic products. The predictions are presented in the form of a Table and shown to have concordance with experimental results.
Chelvanayagam
G
G
John Curtin School of Medical Research, Australian National University, Canberra. Gareth.Chelva@anu.edu.au
D000483:Alleles; D000918:Antibody Specificity / Q000276:immunology / Q000502:physiology*; D001665:Binding Sites / Q000502:physiology; D005802:Genes, MHC Class II / Q000502:physiology; D006684:HLA-DR Antigens / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D010449:Peptide Mapping; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation
D006684:HLA-DR Antigens; D010455:Peptides